Selected article for: "amino acid and directly bind"

Author: Kuban-Jankowska, Alicja; Sahu, Kamlesh K; Niedzialkowski, Pawel; Gorska, Magdalena; Tuszynski, Jack A; Ossowski, Tadeusz; Wozniak, Michal
Title: Redox process is crucial for inhibitory properties of aurintricarboxylic acid against activity of YopH: virulence factor of Yersinia pestis
  • Document date: 2015_7_22
  • ID: 1irvzt8v_37
    Snippet: The docking studies showed that ATA bonds specifically in the active site of YopH. ATA can accommodate itself well inside the binding site as compared to pTyr and that may be the reason for a higher binding affinity of ATA to YopH and ATA as compared to pTyr. By performing molecular dynamics simulations of the complex we found that two carboxyl groups of ATA bind directly toward the essential amino-acid residues for enzyme catalysis in the active.....
    Document: The docking studies showed that ATA bonds specifically in the active site of YopH. ATA can accommodate itself well inside the binding site as compared to pTyr and that may be the reason for a higher binding affinity of ATA to YopH and ATA as compared to pTyr. By performing molecular dynamics simulations of the complex we found that two carboxyl groups of ATA bind directly toward the essential amino-acid residues for enzyme catalysis in the active site. Cys403 and Arg409 are involved in the reaction of dephosphorylation of substrate on tyrosine residues. The binding conformation of ATA in the YopH active site contributed to the relatively strong calculated binding affinity of ATA in comparison to natural substrate.

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